title: Differential binding of lectins IL-2 and CSL to candida albicans and cancer cells.
abstract: The demonstration that interleukin 2 (IL-2) is a lectin specific for oligomannosides allows to understand a new function for this cytokine: as a bifunctional molecule when bound to its receptor ss, IL-2 associates the latter which the CD3/TCR complex, interacting with oligosaccharides of CD3 through its carbohydrate-recognition domain (Zanetta et al. , 1996, Biochem. J., 318, 49-53). This induces the tyrosine phosphorylation of the IL-2R beta by ++p56(lck) , the first step of the IL-2-dependent signaling. Since this specific association is disrupted in vitro by oligomannosides with five and six mannose residues, we made the hypothesis that pathogenic cells or microorganisms could bind IL-2, consequently disturbing the IL-2-dependent response. This study shows that the pathogenic yeast Candida albicans (in contrast with nonpathogenic yeasts) binds high amounts of IL-2 as did cancer cells. In contrast with cancer cells, yeasts do not bind the Man6GlcNAc2-specific lectin CSL, an endogenous "amplifier of activation signals" (Zanetta et al. , 1995, Biochem. J., 311, 629-636).
authors.affiliation: Laboratoire de Chimie Biologique, Cedex, France.
authors.forename: J P
authors.initials: JP
authors.lastname: Zanetta
authors.forename: R
authors.initials: R
authors.lastname: Bonaly
authors.forename: S
authors.initials: S
authors.lastname: Maschke
authors.forename: G
authors.initials: G
authors.lastname: Strecker
authors.forename: J C
authors.initials: JC
authors.lastname: Michalski
mesh_terms: D019921:Biotinylation; D017252:CD3 Complex / Q000378:metabolism; D002176:Candida albicans / Q000378:metabolism* / Q000472:pathogenicity; D002473:Cell Wall / Q000737:chemistry; D005909:Glioblastoma / Q000378:metabolism*; D019302:HIV Envelope Protein gp160 / Q000378:metabolism; D006801:Humans; D007376:Interleukin-2 / Q000378:metabolism*; D007716:Kluyveromyces / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / Q000378:metabolism; D008351:Mannans / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D010766:Phosphorylation; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D015375:Receptors, Interleukin-2 / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012440:Saccharomyces / Q000378:metabolism; D012568:Schizosaccharomyces / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D017252:CD3 Complex; D019302:HIV Envelope Protein gp160; D007376:Interleukin-2; D037102:Lectins; D008351:Mannans; D008562:Membrane Glycoproteins; D011948:Receptors, Antigen, T-Cell; D015375:Receptors, Interleukin-2; D011994:Recombinant Proteins; C064465:mannosyl(6)-N-acetylglucosamine(2); D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck)